Investigation of the catalytic triad of arylamine N-acetyltransferases: essential residues required for acetyl transfer to arylamines.
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Arylamine N-acetyltransferases: from drug metabolism and pharmacogenetics to drug discoveryProbing the architecture of the Mycobacterium marinum arylamine N-acetyltransferase active siteStructural and Biochemical Characterization of an Active Arylamine N-Acetyltransferase Possessing a Non-canonical Cys-His-Glu Catalytic TriadKinetic and chemical mechanism of arylamine N-acetyltransferase from Mycobacterium tuberculosisKinetic characterisation of arylamine N-acetyltransferase from Pseudomonas aeruginosa.Probing the catalytic potential of the hamster arylamine N-acetyltransferase 2 catalytic triad by site-directed mutagenesis of the proximal conserved residue, Tyr190.Analysis of novel soluble chromate and uranyl reductases and generation of an improved enzyme by directed evolutionFunctional characterization of the A411T (L137F) and G364A (D122N) genetic polymorphisms in human N-acetyltransferase 2.Functional characterization of single-nucleotide polymorphisms and haplotypes of human N-acetyltransferase 2.Arylamine N-acetyltransferases.Structure/function evaluations of single nucleotide polymorphisms in human N-acetyltransferase 2Arylamine N-acetyltransferases in mycobacteria.Update on the pharmacogenetics of NATs: structural considerations.Crystal structure of arylamine N-acetyltransferases: insights into the mechanisms of action and substrate selectivity.Arylamine N-acetyltransferases: a structural perspective.Understanding Protein Palmitoylation: Biological Significance and EnzymologyPurification, crystallization and preliminary X-ray characterization of Bacillus cereus arylamine N-acetyltransferase 3 [(BACCR)NAT3].Reaction mechanism of azoreductases suggests convergent evolution with quinone oxidoreductases.Binding of the anti-tubercular drug isoniazid to the arylamine N-acetyltransferase protein from Mycobacterium smegmatis.Reversibly acetylated lysine residues play important roles in the enzymatic activity of Escherichia coli N-hydroxyarylamine O-acetyltransferase.A low-barrier hydrogen bond mediates antibiotic resistance in a noncanonical catalytic triad.
P2860
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P2860
Investigation of the catalytic triad of arylamine N-acetyltransferases: essential residues required for acetyl transfer to arylamines.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
Investigation of the catalytic ...... acetyl transfer to arylamines.
@en
type
label
Investigation of the catalytic ...... acetyl transfer to arylamines.
@en
prefLabel
Investigation of the catalytic ...... acetyl transfer to arylamines.
@en
P2093
P2860
P356
P1433
P1476
Investigation of the catalytic ...... acetyl transfer to arylamines.
@en
P2093
Adeel Mushtaq
James Sandy
Pamela Schartau
Simon J Holton
P2860
P304
P356
10.1042/BJ20050277
P407
P577
2005-08-01T00:00:00Z